ID   BODG_CAEEL              Reviewed;         421 AA.
AC   Q19000;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Probable gamma-butyrobetaine dioxygenase;
DE            EC=1.14.11.1;
DE   AltName: Full=Gamma-butyrobetaine hydroxylase;
DE            Short=Gamma-BBH;
DE   AltName: Full=Gamma-butyrobetaine,2-oxoglutarate dioxygenase;
GN   Name=gbh-1; ORFNames=D2089.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the formation of L-carnitine from gamma-
CC       butyrobetaine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine
CC         + CO2 + succinate; Xref=Rhea:RHEA:24028, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16244, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17126, ChEBI:CHEBI:30031; EC=1.14.11.1;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC   -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
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DR   EMBL; Z36948; CAA85412.1; -; Genomic_DNA.
DR   PIR; T20380; T20380.
DR   RefSeq; NP_496305.1; NM_063904.6.
DR   AlphaFoldDB; Q19000; -.
DR   SMR; Q19000; -.
DR   STRING; 6239.D2089.5; -.
DR   EPD; Q19000; -.
DR   PaxDb; Q19000; -.
DR   PeptideAtlas; Q19000; -.
DR   PRIDE; Q19000; -.
DR   EnsemblMetazoa; D2089.5.1; D2089.5.1; WBGene00001522.
DR   GeneID; 174648; -.
DR   KEGG; cel:CELE_D2089.5; -.
DR   UCSC; D2089.5; c. elegans.
DR   CTD; 174648; -.
DR   WormBase; D2089.5; CE00940; WBGene00001522; gbh-1.
DR   eggNOG; KOG3888; Eukaryota.
DR   GeneTree; ENSGT00530000063582; -.
DR   HOGENOM; CLU_021859_2_0_1; -.
DR   InParanoid; Q19000; -.
DR   OMA; SVNILHC; -.
DR   OrthoDB; 868657at2759; -.
DR   PhylomeDB; Q19000; -.
DR   Reactome; R-CEL-71262; Carnitine synthesis.
DR   UniPathway; UPA00118; -.
DR   PRO; PR:Q19000; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00001522; Expressed in embryo and 4 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008336; F:gamma-butyrobetaine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0045329; P:carnitine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.30.2020.30; -; 1.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR012775; GBBH.
DR   InterPro; IPR038492; GBBH-like_N_sf.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   Pfam; PF02668; TauD; 1.
DR   TIGRFAMs; TIGR02409; carnitine_bodg; 1.
PE   3: Inferred from homology;
KW   Carnitine biosynthesis; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..421
FT                   /note="Probable gamma-butyrobetaine dioxygenase"
FT                   /id="PRO_0000207088"
FT   BINDING         222
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  48436 MW;  10949C4BF8262DF6 CRC64;
     MLSALLIRNI RNASKLASVA GPNSDRIVNV KWSDGKTGVF PLIWLRDTSP DPSTYTISPA
     MTARKLTMLE FDVEQNARKL WIDEDANCLK IEWESGVLSE FPSEWLKIRN PSDQEARRRR
     RKVYLFPEQT WGKAEIEGKL KKFSHEEFMK NEQVVHDFLQ AVCIDGIAVL KGAPQGVRGA
     VEAIGDRIGM IKRTHFGLVF EVSLKADASN MAYASNGGLP FHTDFPSLSH PPQLQMLHML
     QSAEEGGHSL FVDGFHVAEQ LRVEKPEIFK ILTTQSMEYI EEGYDVHEIN GKTIRFDYDM
     CARHKVIRLN DDGKVNKIQF GNAMRSWFYD CEPSKVQDVY RAMKTFTEYC YQPRNMLKFR
     LEDGDTVLWA NQRLLHTRDG FRNAPEKART LTGCYFDWDI VKSRVRFLRD KLSLEQNQPS
     A